Cloned (Comment) | Organism |
---|---|
gene MGG_08499, DNA and amino acid sequence determination and analysis, recombinant expression and secretion of the enzyme in Pichia pastoris | Pyricularia oryzae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kineticss | Pyricularia oryzae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | enzyme-bound, is eliminated by denaturation of the enzyme protein | Pyricularia oryzae | |
Fe2+ | required, low amount bound to the enzyme | Pyricularia oryzae | |
Mn2+ | required, high amount bound to the enzyme, exogenous Mn2+ does not enhance the enzyme activity | Pyricularia oryzae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyricularia oryzae | G4NAP4 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the deglycosylation process reduces the recombinant enzyme activity, but more than 50% is retained | Pyricularia oryzae |
Purification (Comment) | Organism |
---|---|
recombinant secreted enzyme 43fold from Pichia pastoris by hydrophobic interaction chromatography and gel filtration | Pyricularia oryzae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2.01 | - |
purified recombinant enzyme, pH 9.0, 21°C | Pyricularia oryzae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-dilinoleoyl-phosphatidylcholine + O2 | a poor substrate | Pyricularia oryzae | ? | - |
? | |
1-linoleoyl-2-hydroxy-phosphatidylcholine + O2 | an excellent substrate | Pyricularia oryzae | ? | - |
? | |
linoleate + O2 | - |
Pyricularia oryzae | (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate | - |
? | |
lyso-phosphatidylcholine + O2 | substrate from soybean | Pyricularia oryzae | ? | - |
? | |
additional information | the enzyme can also convert linoleate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate, cf. linoleate 9S-lipoxygenase/EC 1.13.11.58 and linoleate 13R-lipoxygenase. Oxygen consumption monitoring | Pyricularia oryzae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 11000-130000, glycosylated recombinant enzyme, SDS-PAGE, x * 70000, about, deglycosylated recombinant enzyme, SDS-PAGE | Pyricularia oryzae |
Synonyms | Comment | Organism |
---|---|---|
manganese lipoxygenase | - |
Pyricularia oryzae |
MGG_08499 | - |
Pyricularia oryzae |
MnLOX | - |
Pyricularia oryzae |
Mo-MnLOX | - |
Pyricularia oryzae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
21 | - |
assay at | Pyricularia oryzae |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
the deglycosylation process slightly decreases the melting temperature of recombinant Mo-MnLOX from 60°C to 56°C | Pyricularia oryzae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
assay at | Pyricularia oryzae |